{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T19:25:18Z","timestamp":1791141918279,"version":"4.1.0"},"reference-count":18,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2011,11,14]],"date-time":"2011-11-14T00:00:00Z","timestamp":1321228800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2012,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Abnormal fibrillization of amyloidogenic peptides\/proteins has been linked to various neurodegenerative diseases such as Alzheimer's and Parkinson's disease as well as with type\u2010II diabetes mellitus. The kinetics of protein fibrillization is commonly studied by using a fluorescent dye Thioflavin T (ThT) that binds to protein fibrils and exerts increased fluorescence intensity in bound state. Recently, it has been demonstrated that several low\u2010molecular weight compounds like Basic Blue 41, Basic Blue 12, Azure C, and Tannic acid interfere with the fluorescence of ThT bound to Alzheimers' amyloid\u2010<jats:italic>\u03b2<\/jats:italic> fibrils and cause false positive results during the screening of fibrillization inhibitors. In the current study, we demonstrated that the same selected substances also decrease the fluorescence signal of ThT bound to insulin fibrils already at submicromolar or micromolar concentrations. Kinetic experiments show that unlike to true inhibitors, these compounds did neither decrease the fibrillization rate nor increase the lag\u2010period. Absence of soluble insulin in the end of the experiment confirmed that these compounds do not disaggregate the insulin fibrils and, thus, are not fibrillization inhibitors at concentrations studied. Our results show that interference with ThT test is a general phenomenon and more attention has to be paid to interpretation of kinetic results of protein fibrillization obtained by using fluorescent dyes. Copyright \u00a9 2011 European Peptide Society and John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/psc.1416","type":"journal-article","created":{"date-parts":[[2011,11,15]],"date-time":"2011-11-15T14:37:56Z","timestamp":1321367876000},"page":"59-64","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":38,"title":["Interference of low\u2010molecular substances with the thioflavin\u2010T fluorescence assay of amyloid fibrils"],"prefix":"10.1002","volume":"18","author":[{"given":"Andra","family":"Noorm\u00e4gi","sequence":"first","affiliation":[{"name":"Department of Gene Technology Tallinn University of Technology  Akadeemia 15 12618 Tallinn Estonia"},{"name":"Competence Center on Reproductive Medicine and Biology  Tiigi 61b Tartu 50410 Estonia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kateryna","family":"Primar","sequence":"additional","affiliation":[{"name":"Department of Gene Technology Tallinn 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